scholarly journals Fibronectin–collagen binding and requirement during cellular adhesion

1980 ◽  
Vol 186 (2) ◽  
pp. 551-559 ◽  
Author(s):  
Leslie I. Gold ◽  
Edward Pearlstein
Keyword(s):  
Chick Embryo ◽  
Human Plasma ◽  
Hydrophobic Interactions ◽  
Human Fibroblasts ◽  
Sodium Dodecyl ◽  
Cellular Adhesion ◽  
Adhesion Assay ◽  
Human Umbilical Cord ◽  
Ionic Detergents ◽  
Kinetics Of

Fibronectin isolated from human plasma and from the extracellular matrices of cell monolayers mediates the attachment in vitro and spreading of trypsin-treated cells on a collagen substratum. Fibronectin-dependent kinetics of cellular attachment to collagen were studied for several adherent cell types. It was shown that trypsin-treated human umbilical-cord cells, mouse sarcoma CMT81 cells, endothelial cells, and human fibroblasts from a patient with Glanzmann's disease were completely dependent on fibronectin for their attachment to collagen, whereas guinea-pig and monkey smooth-muscle cells and chick-embryo secondary fibroblasts displayed varying degrees of dependence on fibronectin for their attachment. Radiolabelled human plasma fibronectin possessed similar affinity for collagen types I, II and III from a variety of sources. The fibronectin bound equally well to the collagens with or without prior urea treatment. However, in the fibronectin-mediated adhesion assay using PyBHK fibroblasts, a greater number of cells adhered and more spreading was observed on urea-treated collagen. Fibronectin extracted from the extracellular matrix of chick-embryo fibroblasts and that purified from human plasma demonstrated very similar kinetics of complexing to collagencoated tissue-culture dishes. Fibronectin from both sources bound to collagen in the presence of 0.05–4.0m-NaCl and over the pH range 2.6–10.6. The binding was inhibited when fibronectin was incubated with 40–80% ethylene glycol, the ionic detergents sodium dodecyl sulphate and deoxycholate, and the non-ionic detergents Nonidet P-40, Tween 80 and Triton X-100, all at a concentration of 0.1%. From these results we proposed that fibronectin–collagen complexing is mainly attributable to hydrophobic interactions.

scholarly journals Influence of surfactants on the fading of malachite green

2008 ◽  
Vol 6 (1) ◽  
pp. 89-92 ◽  
Author(s):  
Adina Raducan ◽  
Alexandra Olteanu ◽  
Mihaela Puiu ◽  
Dumitru Oancea
Keyword(s):  
Malachite Green ◽  
Anionic Surfactant ◽  
Cationic Surfactants ◽  
Hydrophobic Interactions ◽  
Sodium Dodecyl ◽  
Inhibitory Effect ◽  
Dimethyl Ammonium Chloride ◽  
Electrostatic And Hydrophobic Interactions ◽  
Dimethyl Ammonium ◽  
Kinetics Of

AbstractThe kinetics of the reaction between malachite green (MG) and sodium hydroxide (MG fading) was studied using a spectrophotometric method in the presence of two cationic surfactants, cetyl-benzyl-dimethyl-ammonium chloride (CBDAC) and hexadecyl-trimethylammonium bromide (HTAB) and one anionic surfactant, sodium dodecyl sulphate (SDS) at concentrations below and above critical micellar concentrations. The cationic surfactants have a catalytic effect, while the anionic surfactant has an inhibitory effect on the reaction. A kinetic model describing the influence of surfactant on reaction rate was developed. The results are discussed on the basis of electrostatic and hydrophobic interactions between the kinetic micelles and malachite green.

scholarly journals Essential charged amino acids in the binding of fibronectin to gelatin

1982 ◽  
Vol 201 (1) ◽  
pp. 1-8 ◽  
Author(s):  
M Vuento ◽  
E Salonen ◽  
K Osterlund ◽  
U H Stenman
Keyword(s):  
Hydrophobic Interactions ◽  
Sodium Dodecyl ◽  
Sodium Deoxycholate ◽  
Binding Activity ◽  
Tween 20 ◽  
Ph Optimum ◽  
Ionic Detergents ◽  
Charged Amino Acids ◽  
Triton X

The binding of fibronectin to gelatin-agarose was strictly dependent on pH, having a pH optimum of 7-9. The binding was strongly inhibited by increasing ionic strength. A chemical modification of lysyl and arginyl groups of fibronectin abolished the binding activity. The anionic detergents sodium dodecyl sulphate and sodium deoxycholate in concentrations of 10-100mM had the same effect. The binding was not affected by the non-ionic detergents Triton X-100, Tween 20 or Lubrol WX. The results demonstrate an important role of ionic interactions in the binding of fibronectin to gelatin. Absence of inhibition by non-ionic detergents suggests that hydrophobic interactions contribute relatively little to the binding of fibronectin to gelatin.

scholarly journals Engineering of Bio-Adhesive Ligand Containing Recombinant RGD and PHSRN Fibronectin Cell-Binding Domains in Fusion with a Colored Multi Affinity Tag: Simple Approach for Fragment Study from Expression to Adsorption

2021 ◽  
Vol 22 (14) ◽  
pp. 7362
Author(s):  
Amina Ben Abla ◽  
Guilhem Boeuf ◽  
Ahmed Elmarjou ◽  
Cyrine Dridi ◽  
Florence Poirier ◽  
...  
Keyword(s):  
Specific Binding ◽  
Cellular Adhesion ◽  
High Yield ◽  
Adhesion Assay ◽  
Cell Binding ◽  
Affinity Tag ◽  
Binding Domains ◽  
Rational Development ◽  
Fibronectin Type Iii ◽  
Arginine Glycine Aspartic Acid

Engineering of biomimetic motives have emerged as promising approaches to improving cells’ binding properties of biomaterials for tissue engineering and regenerative medicine. In this study, a bio-adhesive ligand including cell-binding domains of human fibronectin (FN) was engineered using recombinant protein technology, a major extracellular matrix (ECM) protein that interacts with a variety of integrins cell-surface’s receptors and other ECM proteins through specific binding domains. 9th and 10th fibronectin type III repeat containing Arginine-Glycine-Aspartic acid (RGD) and Pro-His-Ser-Arg-Asn (PHSRN) synergic site (FNIII9-10) were expressed in fusion with a Colored Multi Affinity Tag (CMAT) to develop a simplified production and characterization process. A recombinant fragment was produced in the bacterial system using E. coli with high yield purified protein by double affinity chromatography. Bio-adhesive surfaces were developed by passive coating of produced fragment onto non adhesive surfaces model. The recombinant fusion protein (CMAT-FNIII9/10) demonstrated an accurate monitoring capability during expression purification and adsorption assay. Finally, biological activity of recombinant FNIII9/10 was validated by cellular adhesion assay. Binding to α5β1 integrins were successfully validated using a produced fragment as a ligand. These results are robust supports to the rational development of bioactivation strategies for biomedical and biotechnological applications.

The Kinetics of Methyl Methacrylate Miniemulsion Polymerization Characterized through a Fluorescence Method

2012 ◽  
Vol 178-181 ◽  
pp. 609-612
Author(s):  
Hai Ke Feng ◽  
Hua Yu Qiu ◽  
Li Yuan Ding ◽  
Cun Jin Xu
Keyword(s):  
Methyl Methacrylate ◽  
Anionic Surfactant ◽  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Miniemulsion Polymerization ◽  
Time Measurement ◽  
Fluorescence Method ◽  
Real Time Measurement ◽  
Measurement Results ◽  
Kinetics Of

In this paper, we followed the kinetics of methyl methacrylate (MMA) through a novel fluorescence method. The real-time measurement results show that in the regime of very low monomer contents, such as a solution containing 0.1 wt% of MMA with respect to water and with the anionic surfactant of sodium dodecyl sulphate (SDS), the kinetic of the miniemulsion could be followed by this embed fluorescence method. The processes of changing from emulsion to miniemulsion with different amount of surfactant and cosurfactant also have been monitored.

Solubilization and immunoprecipitation of 125I-labelled antigens from Plasmodium knowlesi schizont-infected erythrocytes using non-ionic, anionic and zwitterionic detergents

Parasitology ◽  
1984 ◽  
Vol 88 (1) ◽  
pp. 27-36 ◽  
Author(s):  
R. J. Howard ◽  
J. W. Barnwell
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Plasmodium Knowlesi ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein A ◽  
Sodium Dodecyl ◽  
Ionic Detergents ◽  
Class A ◽  
Anionic Detergents ◽  
Triton X

SUMMARYPlasmodium knowlesi malaria-infected erythrocytes were radio-iodinated and several non-ionic, anionic and zwitterionic detergents were compared in their capacity to extract the labelled membrane proteins. The use of these detergents for antigen identification was tested by immunoprecipitation, after addition of Triton X-100 to some detergent extracts, using hyperimmune monkey antiserum and protein A-Sepharose. 125I-labelled antigens were specifically immunoprecipitated with all detergents tested, including the anionic detergents sodium dodecyl sulphate (SDS), deoxycholate and cholate; the zwitterions Zwittergent-312 and -314, CHAPS and Empigen BB, as well as several non-ionic detergents. The SDS-polyacrylamide gel electrophoresis patterns of 125I-labelled antigens varied after extraction with different detergents, there being no consistent pattern for detergents of a particular class. A total of 14 125I-labelled antigens were identified, 11 of them using Triton X-100. Some minor antigens identified with Triton X-100 were immunoprecipitated in greater amount after extraction in other detergents. Most importantly, two antigens Mr 200000 and 180000 were detected only after extraction with deoxycholate or SDS.

Coordinate induction of metallothioneins I and II in rodent cells by UV irradiation

1988 ◽  
Vol 8 (11) ◽  
pp. 4716-4720
Author(s):  
A J Fornace ◽  
H Schalch ◽  
I Alamo
Keyword(s):  
Sequence Analysis ◽  
Uv Irradiation ◽  
Time Course ◽  
Human Fibroblasts ◽  
Chinese Hamster ◽  
Cdna Clones ◽  
X Rays ◽  
General Stress Response ◽  
Rapid Induction ◽  
Kinetics Of

Sequence analysis of Chinese hamster V79 lung fibroblast cDNA clones, which code for UV radiation-inducible transcripts, revealed that many of the clones corresponded to metallothioneins (MTs) I and II. A third cDNA clone, DDIU4, was found also to code for a similar-size UV-inducible transcript which was unrelated to MT by both sequence analysis and kinetics of induction. MTI and MTII RNAs rapidly increased in V79 cells within 1 h after UV irradiation, and maximum induction was seen by 4 h. This rapid induction of MT RNA by UV irradiation was not observed in human fibroblasts. MTI and MTII were coordinately induced in both time course and dose-response experiments, although the induction of MTII, up to 30-fold, was three to four times greater than that of MTI. The induction of MT did not appear to be a general stress response, since no increase occurred after exposure to X rays or H2O2.

Changes in the transferrin requirement of cultured chick embryo mesoderm cells during early differentiation

Development ◽  
1986 ◽  
Vol 95 (1) ◽  
pp. 81-93
Author(s):  
E. J. Sanders
Keyword(s):  
Chick Embryo ◽  
Type I Collagen ◽  
Specific Effect ◽  
Primitive Streak ◽  
Cellular Adhesion ◽  
Type I ◽  
Surface Binding ◽  
Surface Receptors ◽  
Early Differentiation ◽  
Species Specific

Mesodermal tissue from the chick embryo at various stages of early differentiation was cultured in hydrated gels of type I collagen in the presence and absence of transferrin. Primary mesoderm explants from primitive-streak-stage embryos responded to the presence of avian transferrin by significantly improved outgrowth which appeared to be related to the ability of the cells to attach to, and migrate in, the collagen. No evidence was obtained which suggested that this observation was dependent on increased cell proliferation. This outgrowth enhancement was not duplicated by transferrin of human origin. The avian transferrin did not produce this effect on cells cultured on plastic substrata, suggesting that the species-specific effect involves modulation by the extracellular matrix. Mesoderm explants from somite stages of development showed no increase in outgrowth in the presence of either avian or human transferrin as judged by counting the number of outwandering cells. Ultrastructural immunocytochemistry indicated surface binding of transferrin by cells in the gels, and the presence of endogenous transferrin on the surfaces of mesoderm cells in situ and in their extracellular environment. It is suggested that by binding to cell surface receptors, transferrin may be able to influence the strength of cellular adhesion to collagen and hence the capacity for cell locomotion.

Mobility of DR1 Molecules Embedded in Nanostructured PMMA Films

2009 ◽  
Vol 5 ◽  
pp. 135-142
Author(s):  
Jorge A. García-Macedo ◽  
A. Franco ◽  
Guadalupe Valverde-Aguilar ◽  
M.A. Ríos-Enríquez
Keyword(s):  
Second Harmonic ◽  
Sodium Dodecyl ◽  
Orientation Distribution ◽  
Decay Rates ◽  
Ammonium Bromide ◽  
X Ray Diffraction ◽  
Poling Field ◽  
Different Temperatures ◽  
Cetyl Trimethyl Ammonium ◽  
Kinetics Of

The kinetics of the orientation of Disperse Red 1 (DR1) molecules embedded in nanostructured Polymethylmetacrylate (PMMA) films was studied under the effect of an intense constant electric poling field. The changes in the orientation distribution of the DR1 molecules were followed by Second Harmonic Generation (SHG) measurements. The SHG signal was recorded as function of time at three different temperatures. We focused on both, the signal increases under the presence of the poling field and the signal decays without the poling field. The studied PMMA films were nanostructured by the incorporation of ionic surfactants as the Sodium Dodecyl Sulfate (SDS) and the Cetyl Trimethyl Ammonium Bromide (CTAB) during their preparation. The kinds of nanostructures obtained in the films were determined by means of X-ray diffraction (XRD) measurements. Substantial differences in signal intensity and in growth and decay rates between amorphous and nanostructured films were found.

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